Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain

Structure and function of the BAH domain in chromatin biology

(2012) Na Yang et al.   CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY

Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes

(2012) Julie K. Monda et al.   STRUCTURE

Structural Basis of Silencing: Sir3 BAH Domain in Complex with a Nucleosome at 3.0 A Resolution

(2011) K.-J. Armache et al.   SCIENCE

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

(2011) D. C. Scott et al.   SCIENCE

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes

(2009) V. Sampath et al.   MOLECULAR AND CELLULAR BIOLOGY

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans

(2009) T. Arnesen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA